1us5: Difference between revisions

As part of a structural genomics project, the crystal structure of a, 314-amino-acid protein encoded by Thermus thermophilus HB8 gene TT1099 was, solved to 1.75 A using the multiple-wavelength anomalous dispersion (MAD), method and a selenomethionine-incorporated protein. The native protein, structure was solved to 1.5 A using the molecular-replacement method. Both, structures revealed a bound ligand, L-glutamate or L-glutamine, and a fold, related to the periplasmic substrate-binding proteins (PSBP). Further, comparative structural analysis with other PSBP-fold proteins revealed the, conservation of the predicted membrane permease binding surface area and, indicated that the T. thermophilus HB8 molecule is most likely to be an, L-glutamate and/or an L-glutamine-binding protein related to the cluster 3, periplasmic receptors. However, the geometry of ligand binding is unique, to the T. thermophilus HB8 molecule.

1US5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus] with GLU and EDO as [http://en.wikipedia.org/wiki/ligands ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1US5 OCA].  

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